Thermitase thermostability

Thermitase, a thermostable extracellular serine protease from the thermophrhc microorganism Thermoactinomyces vulgaris, with an esterase/protease activity ratio >1000 1 shows a broad amino acid side-chain tolerance and cleaves methyl, ethyl, benzyl, ethox-ybenzyl, and ferf-butyl esters from a variety of Nps-, Boc-, Bpoc-, and Z-protected di- and oligopeptides in high yields at pH 8 and 33-55 °C (Scheme 15 ).[28,29,60-62] jjj addition, it is specific for the a-carboxy groups of Asp and Glu. 

STRUCTURE OF THERMITASE, A THERMOSTABLE SERINE PROTEINASE FROM THERMOACTINOMYCES VULGARIS, AND ITS RELATIONSHIP WITH SUBTILISIN-TYPE PROTEINASES... 

It has been hypothesized that thermostability is markedly affected by the solvation of hydrophobic surface residues [20]. In spite of the fact that the surface of thermitase is a little more hydrophobic than the surface of the subtilisin BPN molecule, judging by exposition indexes, thermitase has a higher thermostablity than expected [3]. 

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